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Database: UniProt
Entry: A0A0A3Z4D2_9GAMM
LinkDB: A0A0A3Z4D2_9GAMM
Original site: A0A0A3Z4D2_9GAMM 
ID   A0A0A3Z4D2_9GAMM        Unreviewed;       398 AA.
AC   A0A0A3Z4D2;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Mandelate racemase/muconate lactonizing protein {ECO:0000313|EMBL:KGT92481.1};
GN   ORFNames=NG99_13875 {ECO:0000313|EMBL:KGT92481.1};
OS   Erwinia typographi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=371042 {ECO:0000313|EMBL:KGT92481.1, ECO:0000313|Proteomes:UP000030351};
RN   [1] {ECO:0000313|EMBL:KGT92481.1, ECO:0000313|Proteomes:UP000030351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M043b {ECO:0000313|EMBL:KGT92481.1,
RC   ECO:0000313|Proteomes:UP000030351};
RA   Chan K.-G., Tan W.-S.;
RT   "Genome sequence of Erwinia typographi M043b.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR633978-3};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR633978-3};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGT92481.1}.
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DR   EMBL; JRUQ01000040; KGT92481.1; -; Genomic_DNA.
DR   RefSeq; WP_034893851.1; NZ_JRUQ01000040.1.
DR   AlphaFoldDB; A0A0A3Z4D2; -.
DR   STRING; 371042.NG99_13875; -.
DR   eggNOG; COG4948; Bacteria.
DR   OrthoDB; 9796450at2; -.
DR   Proteomes; UP000030351; Unassembled WGS sequence.
DR   GO; GO:0008867; F:galactarate dehydratase activity; IEA:InterPro.
DR   GO; GO:1990594; F:L-altrarate dehydratase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
DR   CDD; cd03316; MR_like; 1.
DR   Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR   Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR033978; L-talarate_dehydratase.
DR   InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   InterPro; IPR046945; RHMD-like.
DR   PANTHER; PTHR13794; ENOLASE SUPERFAMILY, MANDELATE RACEMASE; 1.
DR   PANTHER; PTHR13794:SF58; MITOCHONDRIAL ENOLASE SUPERFAMILY MEMBER 1; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDS00001; Enolase; 1.
DR   SFLD; SFLDF00134; L-talarate/galactarate_dehydra; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR   PROSITE; PS00909; MR_MLE_2; 1.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|PIRSR:PIRSR633978-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR633978-3}.
FT   DOMAIN          176..273
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        197
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-1"
FT   ACT_SITE        328
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-1"
FT   BINDING         46..48
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT   BINDING         82..83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT   BINDING         226
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT   BINDING         252
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT   BINDING         278
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT   BINDING         348
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT   SITE            301
FT                   /note="Increases basicity of active site His"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633978-4"
SQ   SEQUENCE   398 AA;  44053 MW;  E8B00D2F35A1A049 CRC64;
     MSLSANSEAV TYAKVAHAKT AAETGDRIEW VQLSLAFLPL ATPVSDAKVL TGRQKPLTEV
     AIIIAEIRSR DGFEGVGFSY SKRAGGQGIY AHAKEIADNL LGEDPNDIDK IYTKLLWAGA
     SVGRSGMAVQ AISPMDIALW DMKAKRAGLP LAKLLGAHRD SVQCYNTSGG FLHTPLEQVL
     KNVVISRENG IGGIKLKVGQ PNCAEDIRRL TAVRQALGED FPLMVDANQQ WDRETAIRMG
     RKMEQFNLIW IEEPLDAYDV EGHAQLAAAL DTPIATGEML TSFREHEQLI LGNASDFVQP
     DAPRVGGISP FLKIMDLAAK HGRKLAPHFA MEVHLHLSAA YPLEPWLEHF EWLNPLFNEQ
     LELRDGRMWI SDRHGLGFTL SEQARRWTQL SCEFGKRP
//
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